Reviewed, UniProtKB/Swiss-Prot P57243 (DYR_BUCAI)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	folA
Ordered Locus Names:	BU143

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 161	161	Dihydrofolate reductase		PRO_0000186383
Regions
	Domain	2 – 161	160	DHFR
	Nucleotide binding	7 – 8	2	NADP By similarity
	Nucleotide binding	15 – 20	6	NADP By similarity
	Nucleotide binding	44 – 47	4	NADP By similarity
	Nucleotide binding	64 – 66	3	NADP By similarity
	Nucleotide binding	96 – 101	6	NADP By similarity
	Region	6 – 8	3	Substrate binding By similarity
Sites
	Binding site	28	1	Substrate By similarity
	Binding site	59	1	Substrate By similarity
	Binding site	115	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57243-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: E3E88CA6FDC70079	FASTA	161	19,053
	10 20 30 40 50 60 MNISLIAAIS KNLVIGYKNK IPWYLPEDLK WFKQKTINKN IIMGRLTWES IKKKPLPMRK 70 80 90 100 110 120 NIVISSNEIK QEGIIWADSI SNAIISAQYN QEIMIIGGAK IYKEMLFYAN KLYLTHIDID 130 140 150 160 IVGDAYFPEY KLYPYWKTLF RKKNTKNKMN PYNYSFEILS R

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12861.1.
RefSeq	NP_239975.1.
3D structure databases
SMR	P57243. Positions 1-161.
ModBase	Search...
Genome annotation databases
GeneID	1109587.
GenomeReviews	Gene locus BU143 in contig BA000003_GR.
KEGG	buc:BU143.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG665708.
OMA	LAHFKRT.
PhylomeDB	P57243.
Enzyme and pathway databases
BioCyc	BSP107806:BU143-MONOMER.
Family and domain databases
InterPro	IPR012259. DHFR. IPR017925. Dihydrofolate_reductase_CS. IPR001796. Dihydrofolate_reductase_dom. [Graphical view]
PANTHER	PTHR11549:SF1. DHFR. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_BUCAI

Accession

Primary (citable) accession number: P57243

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)